3UR3

Structure of the Cmr2 subunit of the CRISPR RNA silencing complex

3UR3 の概要

• エントリーDOI: 10.2210/pdb3ur3/pdb
• 関連するPDBエントリー: 3UNG
• 分子名称: Cmr2dHD, CALCIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: ferredoxin fold, nucleotide-binding, polymerase, cmr complex, unknown function
• 由来する生物種: Pyrococcus furiosus
• 細胞内の位置: Cytoplasm : Q8U1S6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 80291.97

構造登録者

Cocozaki, A.I.,Ramia, N.F.,Shao, Y.,Hale, C.R.,Terns, R.M.,Terns, M.P.,Li, H. (登録日: 2011-11-21, 公開日: 2012-03-21, 最終更新日: 2024-02-28)

主引用文献

Cocozaki, A.I.,Ramia, N.F.,Shao, Y.,Hale, C.R.,Terns, R.M.,Terns, M.P.,Li, H.
Structure of the Cmr2 Subunit of the CRISPR-Cas RNA Silencing Complex.
Structure, 20:545-553, 2012

PubMed Abstract: Cmr2 is the largest and an essential subunit of a CRISPR RNA-Cas protein complex (the Cmr complex) that cleaves foreign RNA to protect prokaryotes from invading genetic elements. Cmr2 is thought to be the catalytic subunit of the effector complex because of its N-terminal HD nuclease domain. Here, however, we report that the HD domain of Cmr2 is not required for cleavage by the complex in vitro. The 2.3Å crystal structure of Pyrococcus furiosus Cmr2 (lacking the HD domain) reveals two adenylyl cyclase-like and two α-helical domains. The adenylyl cyclase-like domains are arranged as in homodimeric adenylyl cyclases and bind ADP and divalent metals. However, mutagenesis studies show that the metal- and ADP-coordinating residues of Cmr2 are also not critical for cleavage by the complex. Our findings suggest that another component provides the catalytic function and that the essential role by Cmr2 does not require the identified ADP- or metal-binding or HD domains in vitro.

PubMed: 22405013
DOI: 10.1016/j.str.2012.01.018

実験手法

X-RAY DIFFRACTION (2.405 Å)